ArticleMolecular biology of the cell2014
Cdk1 promotes cytokinesis in fission yeast through activation of the septation initiation network.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- Characterization of temperature-sensitive alleles of anillin-like Mid1 and polo kinase Plo1 inmicroPublication biology · 2025Article
- Uncoupling of Mitosis and Cytokinesis Upon a Prolonged Arrest in Metaphase Is Influenced by Protein Phosphatases and Mitotic Transcription in Fission Yeast.Frontiers in cell and developmental biology · 2022Article
- Involvement of the septation initiation network in events during cytokinesis in fission yeast.Journal of cell science · 2018Article
- Quantitative Phosphoproteomics Reveals the Signaling Dynamics of Cell-Cycle Kinases in the Fission Yeast Schizosaccharomyces pombe.Cell reports · 2018Article
- Specific detection of fission yeast primary septum reveals septum and cleavage furrow ingression during early anaphase independent of mitosis completion.PLoS genetics · 2018Article
- The price of independence: cell separation in fission yeast.World journal of microbiology & biotechnology · 2016Review
- Comparative biology of cell division in the fission yeast clade.Current opinion in microbiology · 2015Review
- The septation initiation network controls the assembly of nodes containing Cdr2p for cytokinesis in fission yeast.Journal of cell science · 2015Article
- An Extended, Boolean Model of the Septation Initiation Network in S.Pombe Provides Insights into Its Regulation.PloS one · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In Schizosaccharomyces pombe, late mitotic events are coordinated with cytokinesis by the septation initiation network (SIN), an essential spindle pole body (SPB)-associated kinase cascade, which controls the formation, maintenance, and constriction of the cytokinetic ring. It is not fully understood how SIN initiation is temporally regulated, but it depends on the activation of the GTPase Spg1, which is inhibited during interphase by the essential bipartite GTPase-activating protein Byr4-Cdc16. Cells are particularly sensitive to the modulation of Byr4, which undergoes cell cycle-dependent phosphorylation presumed to regulate its function. Polo-like kinase, which promotes SIN activation, is partially responsible for Byr4 phosphorylation. Here we show that Byr4 is also controlled by cyclin-dependent kinase (Cdk1)-mediated phosphorylation. A Cdk1 nonphosphorylatable Byr4 phosphomutant displays severe cell division defects, including the formation of elongated, multinucleate cells, failure to maintain the cytokinetic ring, and compromised SPB association of the SIN kinase Cdc7. Our analyses show that Cdk1-mediated phosphoregulation of Byr4 facilitates complete removal of Byr4 from metaphase SPBs in concert with Plo1, revealing an unexpected role for Cdk1 in promoting cytokinesis through activation of the SIN pathway.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.